The effect of glycosaminoglycans (GAGs) on amyloid aggregation and toxicity.
about
Syndecan-1 in Cancer: Implications for Cell Signaling, Differentiation, and PrognosticationAmyloidogenic propensity of a natural variant of human apolipoprotein A-I: stability and interaction with ligandsHeparin acts as a structural component of β-endorphin amyloid fibrils rather than a simple aggregation promoter.Insights into the consequences of co-polymerisation in the early stages of IAPP and Aβ peptide assembly from mass spectrometry.Inferring Mechanistic Parameters from Amyloid Formation Kinetics by Approximate Bayesian Computation.Chondroitin sulfates and their binding molecules in the central nervous system.Modulation of amyloid assembly by glycosaminoglycans: from mechanism to biological significance.Molecular interactions of amyloid nanofibrils with biological aggregation modifiers: implications for cytotoxicity mechanisms and biomaterial design.Molecular Origins of the Compatibility between Glycosaminoglycans and Aβ40 Amyloid FibrilsUnderstanding co-polymerization in amyloid formation by direct observation of mixed oligomers.How Glycosaminoglycans Promote Fibrillation of Salmon Calcitonin.The Multimerization State of the Amyloid-β42 Amyloid Peptide Governs its Interaction Network with the Extracellular Matrix.Multi-component hybrid hydrogels - understanding the extent of orthogonal assembly and its impact on controlled release.Heparan Sulfate Proteoglycans as Relays of Neuroinflammation.Learning from Synthetic Models of Extracellular Matrix; Differential Binding of Wild Type and Amyloidogenic Human Apolipoprotein A-I to Hydrogels Formed from Molecules Having Charges Similar to Those Found in Natural GAGs.Heparan sulfates facilitate harmless amyloidogenic fibril formation interacting with elastin-like peptides.Effect of the electrostatic surface potential on the oligomerization of full-length human recombinant prion protein at single-molecule level.Heparin promotes fibril formation by the N-terminal fragment of amyloidogenic apolipoprotein A-I.Unravelling the inhibitory activity of Chlamydomonas reinhardtii sulfated polysaccharides against α-Synuclein fibrillation.
P2860
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P2860
The effect of glycosaminoglycans (GAGs) on amyloid aggregation and toxicity.
description
2015 nî lūn-bûn
@nan
2015年の論文
@ja
2015年学术文章
@wuu
2015年学术文章
@zh-cn
2015年学术文章
@zh-hans
2015年学术文章
@zh-my
2015年学术文章
@zh-sg
2015年學術文章
@yue
2015年學術文章
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2015年學術文章
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name
The effect of glycosaminoglycans (GAGs) on amyloid aggregation and toxicity.
@en
type
label
The effect of glycosaminoglycans (GAGs) on amyloid aggregation and toxicity.
@en
prefLabel
The effect of glycosaminoglycans (GAGs) on amyloid aggregation and toxicity.
@en
P2093
P2860
P921
P1433
P1476
The effect of glycosaminoglycans (GAGs) on amyloid aggregation and toxicity.
@en
P2093
Clara Iannuzzi
Gaetano Irace
Ivana Sirangelo
P2860
P304
P356
10.3390/MOLECULES20022510
P407
P577
2015-02-02T00:00:00Z